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Crystal structure of valacyclovir hydrolase complexed with a product analogue

Analyse Crystal structure of valacyclovir hydrolase complexed with a product analogue in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OCI
Type: protein
Length: 254 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Valacyclovir hydrolase
EC: 3.1.-.-
UniProt: Q86WA6
Ligands: TYC, MN, MG
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Valacyclovir hydrolase (EC 3.1.-.-)	protein	254	42% helix, 21% strand	Q86WA6

Ligands and binding sites

TYC · L-tyrosinamide · ligand · chains A
MN · Manganese (II) ion · metal · chains A
MG · Magnesium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	416	0.73	0.83	36	TYC

Compared structures

2OCI · Crystal structure of valacyclovir hydrolase complexed with a product analogue · the same entry in another collection · chain A against A, TM-score 1.00
Q86WA6 · AlphaFold monomer V2.0 prediction for valacyclovir hydrolase (Q86WA6) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q86WA6
Elsewhere: RCSB PDB 2OCI · PDBe 2OCI · UniProt Q86WA6

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